ArticleThe Journal of biological chemistry2013
Engineering visual arrestin-1 with special functional characteristics.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 41 citations in OpenAlex.
- The Functional Role of Gate Loop Residues in Arrestin Binding to GPCRs.International journal of molecular sciences · 2025Article
- The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.International journal of molecular sciences · 2025Article
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Modulating signalling lifetime to optimise a prototypical animal opsin for optogenetic applications.Pflugers Archiv : European journal of physiology · 2023Article
- Expression of Untagged Arrestins in E. coli and Their Purification.Current protocols · 2023Article
- Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements.International journal of molecular sciences · 2023Article
- The Role of Arrestin-1 Middle Loop in Rhodopsin Binding.International journal of molecular sciences · 2022Article
- Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins.International journal of molecular sciences · 2022Review
- Structural evidence for visual arrestin priming via complexation of phosphoinositols.Structure (London, England : 1993) · 2022Article
- The finger loop as an activation sensor in arrestin.Journal of neurochemistry · 2021Article
- Lysine in the lariat loop of arrestins does not serve as phosphate sensor.Journal of neurochemistry · 2021Article
- An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1.The Journal of biological chemistry · 2020Article
- Targeting arrestin interactions with its partners for therapeutic purposes.Advances in protein chemistry and structural biology · 2020Review
- Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.Scientific reports · 2019Article
- Arrestin mutations: Some cause diseases, others promise cure.Progress in molecular biology and translational science · 2019Review
- Arrestins: structural disorder creates rich functionality.Protein & cell · 2018Review
- Molecular Defects of the Disease-Causing Human Arrestin-1 C147F Mutant.Investigative ophthalmology & visual science · 2018Article
- Enhanced Mutant Compensates for Defects in Rhodopsin Phosphorylation in the Presence of Endogenous Arrestin-1.Frontiers in molecular neuroscience · 2018Article
- Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.Cellular signalling · 2017Article
- Functional role of the three conserved cysteines in the N domain of visual arrestin-1.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Arrestin-1 preferentially binds active phosphorylated rhodopsin. Previously, a mutant with enhanced binding to unphosphorylated active rhodopsin (Rh*) was shown to partially compensate for lack of rhodopsin phosphorylation in vivo. Here we showed that reengineering of the receptor binding surface of arrestin-1 further improves the binding to Rh* while preserving protein stability. In mammals, arrestin-1 readily self-associates at physiological concentrations. The biological role of this phenomenon can only be elucidated by replacing wild type arrestin-1 in living animals with a non-oligomerizing mutant retaining all other functions. We demonstrate that constitutively monomeric forms of arrestin-1 are sufficiently stable for in vivo expression. We also tested the idea that individual functions of arrestin-1 can be independently manipulated to generate mutants with the desired combinations of functional characteristics. Here we showed that this approach is feasible; stable forms of arrestin-1 with high Rh* binding can be generated with or without the ability to self-associate. These novel molecular tools open the possibility of testing of the biological role of arrestin-1 self-association and pave the way to elucidation of full potential of compensational approach to gene therapy of gain-of-function receptor mutations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.